Evidence map›Paper›PMID 40703077›Full record

ReviewRSC advances2025

Aminopeptidase N: a multifunctional and promising target in medicinal chemistry.

Oldřich Farsa, Tomáš Uher

Abstract readReview
In one paragraph

Review in RSC advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Review
  2. Cell entry mechanisms of porcine enteric coronaviruses.The Journal of biological chemistry · 2026
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Oldřich FarsaDepartment of Chemical Drugs, Faculty of Pharmacy, Masaryk University Palackého 1946/1 Brno Czech Republic farsao@pharm.muni.cz.ORCID https://orcid.org/0000-0002-0255-7967
Tomáš UherDepartment of Chemical Drugs, Faculty of Pharmacy, Masaryk University Palackého 1946/1 Brno Czech Republic farsao@pharm.muni.cz.ORCID https://orcid.org/0009-0003-3681-1075

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aminopeptidase N (APN) is a zinc metalloproteinase present in almost all types of organisms and has various functions. Many of them are unrelated to its catalytic activity, which is why APN is sometimes classified as a moonlighting enzyme. APN is involved in carcinogenesis and angiogenesis. It also works as an entrance receptor for some coronaviruses and acts as a mediator during skin inflammation. Additionally, APN removes and helps to recycle regulatory proteins including neuropeptides, which is why its inhibitors hold therapeutic potential for a wide range of diseases, making the design and development of such molecules highly desirable. Some of them, such as bestatin or tosedostat, have already been tested as therapeutics with partial success. This article aims to bring an overview of multiple APN functions and implications for various diseases and their inhibitors which have already been prepared, and to suggest areas where the development of inhibitors may be promising in the future.

Identifiers

PMID40703077
PMCPMC12285730

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.